منابع مشابه
Interactions of misfolded influenza virus hemagglutinin with binding protein (BiP)
We have characterized the association between the binding protein, BiP (also known as GRP 78), and misfolded forms of the influenza virus hemagglutinin precursor, HA0. BiP is a heat-shock-related protein that binds to unassembled immunoglobulin heavy chain and to a variety of misfolded proteins in the lumen of the ER. A small fraction (5-10%) of newly synthesized HA0 in CV-1 cells was found to ...
متن کاملBiP and PDI cooperate in the oxidative folding of antibodies in vitro.
Immunoglobulin heavy chain binding protein (BiP), a member of the Hsp70 chaperone family, and the oxidoreductase protein-disulfide isomerase (PDI) play an important role in the folding and oxidation of proteins in the endoplasmic reticulum. However, it was not clear whether both cooperate in this process. We show here that BiP and PDI act synergistically in the in vitro folding of the denatured...
متن کاملBinding Affinity of Antibodies?
Although the switch process is frequently associated with affinity maturation, the constant region is not assumed to play a role in Ag–Ab binding. In the present work, we demonstrate that two clonally related human monoclonal Igs sharing identical V H and V L sequences, but expressing different isotypes (IgA1 k PER and IgG1 k PER ), bind tubulin with significantly different affinities. This dif...
متن کاملSubstrate binding induces depolymerization of the C-terminal peptide binding domain of murine GRP78/BiP.
To investigate the role of each domain in BiP/GRP78 function, we have used a full-length recombinant BiP engineered to contain two enterokinase sites; one site is located after an N-terminal FLAG epitope, and a second site has been inserted at the junction between the N- and C-terminal domains (FLAG-BiP.ent). FLAG-BiP.ent oligomerizes into multiple species that interconvert with each other in a...
متن کاملAntibodies specific to two deoxyribotrinucleotide sequences.
Antibodies to the deoxyribotrinucleotides dpApTpA and dpApApT were prepared by injecting the bovine serum albumin conjugates of the respective haptens in rabbits. The specificities of the antibodies were determined by estimating the inhibition of the binding of the tritiated haptens to the immunoglobulins by various nonradioactive mono- and oligonucleotides, using nitrocellulose membrane bindin...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1995
ISSN: 0021-9258
DOI: 10.1074/jbc.270.46.27589